کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10841190 | 1067884 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A multifunctional galactinol synthase catalyzes the synthesis of fagopyritol A1 and fagopyritol B1 in buckwheat seed
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کلمات کلیدی
RFOd-chiro-inositolRACE-PCRNIDDM5′untranslated regionPCOSRT-PCRIPTGSTSORFGalactosyl cyclitolStachyose synthase5′UTR - 5'UTRGols - اهدافisopropyl β-d-thiogalactoside - ایزوپروپیل β-d-thiogalactosidebase pairs - جفت پایهNon-insulin dependent diabetes mellitus - دیابتی غیر وابسته به انسولینPolycystic ovary syndrome - سندرم تخمدان پلی کیستیکopen reading frame - قاب خواندن بازreverse transcriptase polymerase chain reaction - واکنش زنجیره ای پلی مراز ترانس کریتاز معکوسpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازgalactinol synthase - گالاکتینول سنتاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Fagopyritols are galactosyl cyclitols in buckwheat (Fagopyrum esculentum Moench, Polygonaceae) seeds with structural similarities to a putative insulin mediator deficient in non-insulin dependent diabetes mellitus and polycystic ovary syndrome. Based on the assumption that the multifunctional enzyme galactinol synthase (GolS, UDP-galactose:myo-inositol galactosyltransferase, EC 2.4.1.123) may have homology to the enzyme responsible for the synthesis of fagopyritols, we isolated two full-length and one partial cDNA clones encoding GolS homologues from buckwheat seeds. We designated the genes corresponding to these three cDNAs as Fagopyrum esculentum GolS (FeGolS)-1, FeGolS-2 and FeGolS-3. The full-length FeGolS-1 and FeGolS-2 cDNAs are 1269Â bp and 1326Â bp in length and encode polypeptides of 38.3Â kDa and 40.7Â kDa, respectively. According to the deduced amino acid sequences, FeGolS-1 and FeGolS-2 share a high level of sequence similarity with GolSs in other species. FeGolS-2 and FeGolS-3 contain an insertion of 17 or 18 amino acid residues near the carboxyl terminus, respectively, which is absent in FeGolS-1 and other GolSs. Both bacterially expressed recombinant FeGolS-1 and FeGolS-2 proteins exhibited GolS activities when assayed in the presence of UDP-galactose and myo-inositol. In the presence of UDP-galactose and d-chiro-inositol, FeGolS-1 catalyzed the synthesis of fagopyritol B1 whereas FeGolS-2 catalyzed the synthesis of both fagopyritol A1 and fagopyritol B1 in a 1:4 mole ratio. These results demonstrated that multifunctional GolS homologues in buckwheat seeds confer fagopyritol synthase activities and that the specificity for fagopyritol A1 synthesis may be mediated by a unique class of GolS homologues.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Science - Volume 168, Issue 3, March 2005, Pages 681-690
Journal: Plant Science - Volume 168, Issue 3, March 2005, Pages 681-690
نویسندگان
Takashi Ueda, Mark P. Coseo, Thomas J. Harrell, Ralph L. Obendorf,